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- PDB-1dsj: NMR SOLUTION STRUCTURE OF VPR50_75, 20 STRUCTURES -

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Basic information

Entry
Database: PDB / ID: 1dsj
TitleNMR SOLUTION STRUCTURE OF VPR50_75, 20 STRUCTURES
ComponentsVPR PROTEIN
KeywordsVIRAL PEPTIDE / POLYPEPTIDE
Function / homology
Function and homology information


symbiont-mediated arrest of host cell cycle during G2/M transition / symbiont-mediated activation of host apoptosis / protein homooligomerization / virion component / viral penetration into host nucleus / host cell / monoatomic ion transmembrane transport / host extracellular space / DNA-templated transcription / regulation of DNA-templated transcription ...symbiont-mediated arrest of host cell cycle during G2/M transition / symbiont-mediated activation of host apoptosis / protein homooligomerization / virion component / viral penetration into host nucleus / host cell / monoatomic ion transmembrane transport / host extracellular space / DNA-templated transcription / regulation of DNA-templated transcription / symbiont entry into host cell / host cell nucleus
Similarity search - Function
Retroviral VpR/VpX protein / VPR/VPX protein
Similarity search - Domain/homology
Biological speciesHuman immunodeficiency virus 1
MethodSOLUTION NMR
AuthorsYao, S. / Torres, A.M. / Azad, A.A. / Macreadie, I.G. / Norton, R.S.
Citation
Journal: Protein Pept.Lett. / Year: 1998
Title: Helical structure of polypeptides from the C-terminal half of HIV-1 VPR.
Authors: Yao, S.G. / Azad, A.A. / Macreadie, I.G. / Norton, R.S.
#1: Journal: Proc.Natl.Acad.Sci.USA / Year: 1996
Title: Vpr Protein of Human Immunodeficiency Virus Type 1 Forms Cation-Selective Channels in Planar Lipid Bilayers
Authors: Piller, S.C. / Ewart, G.D. / Premkumar, A. / Cox, G.B. / Gage, P.W.
#2: Journal: Proc.Natl.Acad.Sci.USA / Year: 1995
Title: A Domain of Human Immunodeficiency Virus Type 1 Vpr Containing Repeated H(S/F)Rig Amino Acid Motifs Causes Cell Growth Arrest and Structural Defects
Authors: Macreadie, I.G. / Castelli, L.A. / Hewish, D.R. / Kirkpatrick, A. / Ward, A.C. / Azad, A.A.
History
DepositionOct 23, 1997Processing site: BNL
Revision 1.0Jul 1, 1998Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 16, 2022Group: Database references / Derived calculations / Other
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_struct_assembly / pdbx_struct_oper_list / struct_conn
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.process_site / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id
Revision 1.4Oct 30, 2024Group: Data collection / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / pdbx_entry_details / pdbx_modification_feature

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: VPR PROTEIN


Theoretical massNumber of molelcules
Total (without water)3,0581
Polymers3,0581
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)20 / -
Representative

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Components

#1: Protein/peptide VPR PROTEIN


Mass: 3057.594 Da / Num. of mol.: 1 / Fragment: RESIDUES 50 - 75
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Human immunodeficiency virus 1 / Genus: Lentivirus / References: UniProt: P12520
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR

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Sample preparation

Sample conditionspH: 3.3 / Temperature: 298 K
Crystal grow
*PLUS
Method: other / Details: NMR

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Processing

Software
NameVersionClassification
X-PLOR3.1model building
X-PLOR3.1refinement
X-PLOR3.1phasing
NMR softwareName: X-PLOR / Version: 3.1 / Developer: BRUNGER / Classification: refinement
NMR ensembleConformers submitted total number: 20

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